Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/9346
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Título : Expanding the realm of ultrafast protein folding: gpW, a midsize natural single-domain with α+β topology that folds downhill
Autor : Fung, Adam, Li, Peng, Godoy-Ruiz, Raquel, Sánchez-Ruiz, José M., Muñoz van den Eynde, Víctor
Palabras clave : Protein folding
Ultrafast folding proteins
gpW
Thermodynamic analysis
Downhill folding
Folding barriers
Fecha de publicación : 14-May-2008
Editor: American Chemical Society
Citación : Journal of the American Chemical Society 130(23): 7489-7495 (2008)
Resumen: All ultrafast folding proteins known to date are either very small in size (less than 45 residues), have an α-helix bundle topology, or have been artificially engineered. In fact, many of them share two or even all three features. Here we show that gpW, a natural 62-residue α+β protein expected to fold slowly in a two-state fashion, folds in microseconds (i.e., from τ = 33 µs at 310 K to τ = 1.7 µs at 355 K). Thermodynamic analyses of gpW reveal probe dependent thermal denaturation, complex coupling between two denaturing agents, and differential scanning calorimetry (DSC) thermogram characteristic of folding over a negligible thermodynamic folding barrier. The free energy surface analysis of gpW folding kinetics also produces a marginal folding barrier of about thermal energy (RT) at the denaturation midpoint. From these results we conclude that gpW folds in the downhill regime and is close to the global downhill limit. This protein seems to be poised toward downhill folding by a loosely packed hydrophobic core with low aromatic content, large stabilizing contributions from local interactions, and abundance of positive charges on the native surface. These special features, together with a complex functional role in bacteriophage λ assembly, suggest that gpW has been engineered to fold downhill by natural selection.
Descripción : 7 pages, 5 figures.-- PMID: 18479088 [PubMed].-- Printed version published on Jun 11, 2008.
Versión del editor: http://dx.doi.org/10.1021/ja801401a
URI : http://hdl.handle.net/10261/9346
ISSN: 0002-7863
DOI: 10.1021/ja801401a
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